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- PDB-2bvb: The C-terminal domain from Micronemal Protein 1 (MIC1) from Toxop... -

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Basic information

Entry
Database: PDB / ID: 2bvb
TitleThe C-terminal domain from Micronemal Protein 1 (MIC1) from Toxoplasma Gondii
ComponentsMICRONEMAL PROTEIN 1
KeywordsADHESION / MIC1 / MICRONEME / INVASION
Function / homology
Function and homology information


symbiont-mediated perturbation of host receptor-mediated signal transduction / effector-mediated perturbation of host innate immune response by symbiont / effector-mediated suppression of host innate immune response / Toll-like receptor 2 binding / microneme / Toll-like receptor 4 binding / host cell surface binding / sialic acid binding / immune system process / host cell endosome ...symbiont-mediated perturbation of host receptor-mediated signal transduction / effector-mediated perturbation of host innate immune response by symbiont / effector-mediated suppression of host innate immune response / Toll-like receptor 2 binding / microneme / Toll-like receptor 4 binding / host cell surface binding / sialic acid binding / immune system process / host cell endosome / cytoplasmic vesicle / carbohydrate binding / cell adhesion
Similarity search - Function
Toxoplasma gondii micronemal protein 1 TgMIC1 / Micronemal protein 1 / Micronemal protein 1, galectin-like domain / MIC1, C-terminal superfamily / Toxoplasma gondii micronemal protein 1 TgMIC1 / Micronemal adhesive repeat, sialic-acid binding / Sialic-acid binding micronemal adhesive repeat / Jelly Rolls / Sandwich / Mainly Beta
Similarity search - Domain/homology
Micronemal protein 1
Similarity search - Component
Biological speciesTOXOPLASMA GONDII (eukaryote)
MethodSOLUTION NMR / ARIA
Model type detailsMINIMIZED AVERAGE
AuthorsSaouros, S. / Edwards-Jones, B. / Reiss, M. / Sawmynaden, K. / Cota, E. / Simpson, P. / Dowse, T.J. / Jakle, U. / Ramboarina, S. / Shivarattan, T. ...Saouros, S. / Edwards-Jones, B. / Reiss, M. / Sawmynaden, K. / Cota, E. / Simpson, P. / Dowse, T.J. / Jakle, U. / Ramboarina, S. / Shivarattan, T. / Matthews, S. / Soldati-Favre, D.
CitationJournal: J.Biol.Chem. / Year: 2005
Title: A Novel Galectin-Like Domain from Toxoplasma Gondll Micronemal Protein 1 Assists the Folding, Assembly,and Transport of a Cell-Adhesion Complex.
Authors: Saouros, S. / Edwards-Jones, B. / Reiss, M. / Sawmynaden, K. / Cota, E. / Simpson, P. / Dowse, T.J. / Jakle, U. / Ramboarina, S. / Shivarattan, T. / Matthews, S. / Soldati-Favre, D.
History
DepositionJun 23, 2005Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 12, 2005Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jun 23, 2021Group: Data collection
Category: pdbx_nmr_ensemble / pdbx_nmr_representative ...pdbx_nmr_ensemble / pdbx_nmr_representative / pdbx_nmr_software / pdbx_nmr_spectrometer
Item: _pdbx_nmr_ensemble.conformer_selection_criteria / _pdbx_nmr_ensemble.conformers_calculated_total_number / _pdbx_nmr_software.name
Revision 1.4Nov 6, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: MICRONEMAL PROTEIN 1


Theoretical massNumber of molelcules
Total (without water)14,0311
Polymers14,0311
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / 10structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein MICRONEMAL PROTEIN 1


Mass: 14030.571 Da / Num. of mol.: 1 / Fragment: C-TERMINAL DOMAIN RESIDUES 320-456
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) TOXOPLASMA GONDII (eukaryote) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: O00834
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR detailsText: NONE

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Sample preparation

Sample conditionsTemperature: 310.0 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker OTHERBrukerOTHER5001
Bruker OTHERBrukerOTHER8002

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Processing

NMR software
NameDeveloperClassification
CNSBRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE- KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE,SIMONSON,WARRENrefinement
NMRViewstructure solution
RefinementMethod: ARIA / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 10 / Conformers submitted total number: 1

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